The Journal of Immunology, Vol 139, Issue 3 887-892, Copyright © 1987 by American Association of Immunologists

ARTICLES

Platelet-collagen interaction. Inhibition by a monoclonal antibody raised against collagen receptor

TM Chiang, A Jin and AH Kang

Monoclonal antibodies to the purified platelet type I collagen receptor were produced to study platelet receptor function. The antibody specifically reacted with the platelet receptor in immunoblot experiments. The IgG purified from the monoclonal antibodies and isolated Fab' fragments inhibited the binding of radiolabeled alpha 1(I) chain to washed platelets competitively. Soluble and fibrillar type I collagen-induced platelet aggregations were inhibited by purified IgG suggesting that soluble and fibrillar collagens shared a common receptor. The adhesion of platelets to an artificial collagen matrix was also inhibited by the monoclonal antibody. However, adenosine diphosphate-induced platelet aggregation was not inhibited by the same amount of IgG that inhibited collagen-induced platelet aggregation. The results suggest that collagen-induced platelet aggregation is mediated through the interaction of collagen with the platelet receptor.

This article has been cited by other articles:

				E. Monnet and F. Fauvel-Lafeve A New Platelet Receptor Specific to Type III Collagen. TYPE III COLLAGEN-BINDING PROTEIN J. Biol. Chem., April 6, 2000; 275(15): 10912 - 10917. [Abstract] [Full Text] [PDF]

				P. J. Keely and L. V. Parise The alpha 2beta 1 Integrin Is a Necessary Co-receptor for Collagen-induced Activation of Syk and the Subsequent Phosphorylation of Phospholipase Cgamma 2 in Platelets J. Biol. Chem., October 25, 1996; 271(43): 26668 - 26676. [Abstract] [Full Text] [PDF]